(2S)-2-isopropyl-3-oxosuccinate(2-)

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 酮酸及其衍生物
• 英文名称: (2S)-2-isopropyl-3-oxosuccinate(2-)
• 英文别名: (3S)-2-oxo-3-propan-2-ylbutanedioate
• 化学式: C7H8O5-2
• 分子量: 172.13
• InChiKey: HIIZAGQWABAMRR-BYPYZUCNSA-L

计算性质

• 辛醇/水分配系数(LogP)：
  2
• 重原子数：
  12
• 可旋转键数：
  2
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.57
• 拓扑面积：
  97.3
• 氢给体数：
  0
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  (2S)-2-isopropyl-3-oxosuccinate(2-) 、 氢(+1)阳离子 生成 4-methyl-2-oxopentanoate 、 二氧化碳
  参考文献：
  名称：

  Mirror image mutations reveal the significance of an intersubunit ion cluster in the stability of 3-isopropylmalate dehydrogenase

  摘要：

  The comparison of the three‐dimensional structures of thermophilic (Thermus thermophilus) and mesophilic (Escherichia coli) 3‐isopropylmalate dehydrogenases (IPMDH, EC 1.1.1.85) suggested that the existence of extra ion pairs in the thermophilic enzyme found in the intersubunit region may be an important factor for thermostability. As a test of our assumption, glutamine 200 in the E. coli enzyme was turned into glutamate (Q200E mutant) to mimic the thermophilic enzyme at this site by creating an intersubunit ion pair which can join existing ion clusters. At the same site in the thermophilic enzyme we changed glutamate 190 into glutamine (E190Q), hereby removing the corresponding ion pair. These single amino acid replacements resulted in increased thermostability of the mesophilic and decreased thermostability of the thermophilic enzyme, as measured by spectropolarimetry and differential scanning microcalorimetry.

  DOI：

  10.1016/s0014-5793(00)01190-x
• 作为产物：
  描述：

  (2R,3S)-3-Isopropylmalate 、 nicotinamide adenine dinucleotide 生成 (2S)-2-isopropyl-3-oxosuccinate(2-) 、 氢(+1)阳离子 、 NADH
  参考文献：
  名称：

  Mirror image mutations reveal the significance of an intersubunit ion cluster in the stability of 3-isopropylmalate dehydrogenase

  摘要：

  The comparison of the three‐dimensional structures of thermophilic (Thermus thermophilus) and mesophilic (Escherichia coli) 3‐isopropylmalate dehydrogenases (IPMDH, EC 1.1.1.85) suggested that the existence of extra ion pairs in the thermophilic enzyme found in the intersubunit region may be an important factor for thermostability. As a test of our assumption, glutamine 200 in the E. coli enzyme was turned into glutamate (Q200E mutant) to mimic the thermophilic enzyme at this site by creating an intersubunit ion pair which can join existing ion clusters. At the same site in the thermophilic enzyme we changed glutamate 190 into glutamine (E190Q), hereby removing the corresponding ion pair. These single amino acid replacements resulted in increased thermostability of the mesophilic and decreased thermostability of the thermophilic enzyme, as measured by spectropolarimetry and differential scanning microcalorimetry.

  DOI：

  10.1016/s0014-5793(00)01190-x

文献信息

• The Absolute Configuration of α-carboxyisocaproic Acid (3-Isopropylmalic Acid), an Intermediate in Leucine Biosynthesis^*
  作者：Joseph M. Calvo、Carl M. Stevens、M. G. Kalyanpur、H. E. Umbarger

  DOI：10.1021/bi00900a043

  日期：1964.12.1
• The Biosynthesis of Leucine. III. The Conversion of α-Hydroxy-β-Carboxyisocaproate to α-Ketoisocaproate^*
  作者：R. O. Burns、H. E. Umbarger、S. R. Gross

  DOI：10.1021/bi00905a024

  日期：1963.9.1
• Parsons S.J.; Burns R.O., J Biol Chem, 1969, 0021-9258, 996-1003
  作者：Parsons S.J.、Burns R.O.

  DOI：——

  日期：——